The primary structure of the split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveals an unusual type of diheme cytochrome c

Bart Devreese, Cristina Costa, Hans Demol, Vasilios Papaefthymiou, Isabel Moura, José J. G. Moura, Jozef Van Beeumen

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

The complete amino acid sequence of the unusual diheme split-Soret cytochrome c from the sulphate-reducing Desulfovibrio, desulfuricans strain ATCC 27774 has been determined using classical chemical sequencing techniques and mass spectrometry. The 247-residue sequence shows almost no similarity with any other known diheme cytochrome c, but the heme-binding site of the protein is similar to that of the cytochromes c 3 from the sulphate reducers. The cytochrome-c-like domain of the protein covers only the C-terminal part of the molecule, and there is evidence for at least one more domain containing four cysteine residues, which might bind another cofactor, possibly a non-heme iron-containing cluster. This domain is similar to a sequence fragment of the genome of Archaeoglobus fulgidus, which confirms the high conservation of the genes involved in sulfate reduction.

Original languageEnglish
Pages (from-to)445-451
Number of pages7
JournalEuropean Journal Of Biochemistry
Volume248
Issue number2
DOIs
Publication statusPublished - 1 Jan 1997

Keywords

  • Amino acid sequence
  • Archaeoglobus fulgidus
  • Desulfovibrio
  • Mass spectrometry
  • Sulfate reduction

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